Resolution

Resolution is an average value for the uncertainty of atomic positions in a crystallographic model. High values for resolution (e.g. 5.0 &Aring;) mean high uncertainty, and low values (e.g. 1.0 &Aring;) mean much less uncertainty. 2.05 Å is the median resolution for X-ray crystallographic results in the Protein Data Bank (43,066 on May 2, 2008).

The uncertainty for each atom is quantitated in its temperature value.

The images at right show how the electron density map becomes more accurate and detailed as the uncertainty (resolution value) decreases from 5.0 &Aring; to 0.5 &Aring;.

The images at right were taken from a movie in which the atomic model and electron density map rock back and forth while the resolution value (uncertainty) increases from 0.5 to 5.0 &Aring;. At 0.5 &Aring; in the movie, every atom of the tryptophan sidechain in the top center of the frame is clearly represented by a sphere of electron density. At 2.5 &Aring; (a bit worse than the median in the PDB), the overall shape and position of the Trp sidechain is still clear, as is the alpha helical conformation of the main chain. However, at 5.0 &Aring;, only an ill-fitting bump is present to signal the bulky Trp sidechain, and the alpha helix becomes a cylinder of electron density, from which the handedness of the helix may not be discernable.

Websites

 * Resolution at ProteinExplorer.Org's Glossary.


 * Resolution vs. Electron Density Maps.


 * A Glossary of Terms from Crystallography, NMR, and Homology Modeling